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Inhibitory Effect of Levilactobacillus brevis on Salivary α‐Amylase: Evidence From In Vivo and In Vitro Study.

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Title: Inhibitory Effect of Levilactobacillus brevis on Salivary α‐Amylase: Evidence From In Vivo and In Vitro Study.
Authors: Altamura, Serena1 (AUTHOR), Ciafarone, Alessia1 (AUTHOR), Augello, Francesca Rosaria1 (AUTHOR), Cinque, Benedetta1 (AUTHOR), Pietropaoli, Davide2 (AUTHOR), Palumbo, Paola1 (AUTHOR), Lombardi, Francesca1 (AUTHOR) francesca.lombardi@univaq.it, Henheik, Prisca-Maryla (AUTHOR) phenheik@wiley.com
Source: Journal of Food Biochemistry. 1/24/2026, Vol. 2026, p1-12. 12p.
Subjects: Alpha-amylase, Probiotics, Inhibition (Chemistry), Oral health, In vivo studies, In vitro studies, Lactobacillus, Bioactive compounds
Abstract: Scope: Human salivary α‐amylase (sAA) is a therapeutic target for various pathological oral conditions. Several studies have reported that different probiotic strains can inhibit α‐amylase in vitro. However, the mechanisms behind remain largely unknown. To explore this topic, we focused on Levilactobacillus brevis (L. brevis), a probiotic species known for its beneficial effects on oral health. Methods and Results: The effect of L. brevis on sAA activity was evaluated in vivo by analyzing saliva samples from healthy subjects involved in a randomized, double‐blind, placebo‐controlled study. Additionally, we assessed the effects of probiotic lysate in vitro using a commercial sAA. An amylase‐binding assay was conducted to investigate the interaction between probiotic soluble components and the enzyme. Our findings demonstrate that L. brevis effectively inhibits α‐amylase activity, supporting its positive role in promoting both oral and systemic health. We also observed a similar effect on pancreatic α‐amylase. Conclusion: Our data provide the first evidence of a direct interaction between α‐amylase and bioactive molecules from L. brevis, suggesting that the observed effects could be due to the ability of these probiotic‐derived molecules to bind and inhibit α‐amylase activity. This research expands our understanding of the anticariogenic and antihyperglycemic properties of specific probiotics. Trial Registration: ClinicalTrials.gov identifier: NCT06457724 [ABSTRACT FROM AUTHOR]
Copyright of Journal of Food Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: Inhibitory Effect of Levilactobacillus brevis on Salivary α‐Amylase: Evidence From In Vivo and In Vitro Study.
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  Data: <searchLink fieldCode="AR" term="%22Altamura%2C+Serena%22">Altamura, Serena</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ciafarone%2C+Alessia%22">Ciafarone, Alessia</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Augello%2C+Francesca+Rosaria%22">Augello, Francesca Rosaria</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Cinque%2C+Benedetta%22">Cinque, Benedetta</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Pietropaoli%2C+Davide%22">Pietropaoli, Davide</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Palumbo%2C+Paola%22">Palumbo, Paola</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lombardi%2C+Francesca%22">Lombardi, Francesca</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> francesca.lombardi@univaq.it</i><br /><searchLink fieldCode="AR" term="%22Henheik%2C+Prisca-Maryla%22">Henheik, Prisca-Maryla</searchLink> (AUTHOR)<i> phenheik@wiley.com</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Food+Biochemistry%22">Journal of Food Biochemistry</searchLink>. 1/24/2026, Vol. 2026, p1-12. 12p.
– Name: Subject
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  Data: <searchLink fieldCode="DE" term="%22Alpha-amylase%22">Alpha-amylase</searchLink><br /><searchLink fieldCode="DE" term="%22Probiotics%22">Probiotics</searchLink><br /><searchLink fieldCode="DE" term="%22Inhibition+%28Chemistry%29%22">Inhibition (Chemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Oral+health%22">Oral health</searchLink><br /><searchLink fieldCode="DE" term="%22In+vivo+studies%22">In vivo studies</searchLink><br /><searchLink fieldCode="DE" term="%22In+vitro+studies%22">In vitro studies</searchLink><br /><searchLink fieldCode="DE" term="%22Lactobacillus%22">Lactobacillus</searchLink><br /><searchLink fieldCode="DE" term="%22Bioactive+compounds%22">Bioactive compounds</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Scope: Human salivary α‐amylase (sAA) is a therapeutic target for various pathological oral conditions. Several studies have reported that different probiotic strains can inhibit α‐amylase in vitro. However, the mechanisms behind remain largely unknown. To explore this topic, we focused on Levilactobacillus brevis (L. brevis), a probiotic species known for its beneficial effects on oral health. Methods and Results: The effect of L. brevis on sAA activity was evaluated in vivo by analyzing saliva samples from healthy subjects involved in a randomized, double‐blind, placebo‐controlled study. Additionally, we assessed the effects of probiotic lysate in vitro using a commercial sAA. An amylase‐binding assay was conducted to investigate the interaction between probiotic soluble components and the enzyme. Our findings demonstrate that L. brevis effectively inhibits α‐amylase activity, supporting its positive role in promoting both oral and systemic health. We also observed a similar effect on pancreatic α‐amylase. Conclusion: Our data provide the first evidence of a direct interaction between α‐amylase and bioactive molecules from L. brevis, suggesting that the observed effects could be due to the ability of these probiotic‐derived molecules to bind and inhibit α‐amylase activity. This research expands our understanding of the anticariogenic and antihyperglycemic properties of specific probiotics. Trial Registration: ClinicalTrials.gov identifier: NCT06457724 [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Food Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1155/jfbc/5542445
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 12
        StartPage: 1
    Subjects:
      – SubjectFull: Alpha-amylase
        Type: general
      – SubjectFull: Probiotics
        Type: general
      – SubjectFull: Inhibition (Chemistry)
        Type: general
      – SubjectFull: Oral health
        Type: general
      – SubjectFull: In vivo studies
        Type: general
      – SubjectFull: In vitro studies
        Type: general
      – SubjectFull: Lactobacillus
        Type: general
      – SubjectFull: Bioactive compounds
        Type: general
    Titles:
      – TitleFull: Inhibitory Effect of Levilactobacillus brevis on Salivary α‐Amylase: Evidence From In Vivo and In Vitro Study.
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            – D: 24
              M: 01
              Text: 1/24/2026
              Type: published
              Y: 2026
          Identifiers:
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